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Mol Cell Proteomics ; 18(5): 1027-1035, 2019 05.
Article in English | MEDLINE | ID: mdl-30833379

ABSTRACT

Universal proteomics sample preparation is challenging because of the high heterogeneity of biological samples. Here we describe a novel mechanism that exploits the inherent instability of denatured proteins for nonspecific immobilization on microparticles by protein aggregation capture. To demonstrate the general applicability of this mechanism, we analyzed phosphoproteomes, tissue proteomes, and interaction proteomes as well as dilute secretomes. The findings present a practical, sensitive and cost-effective proteomics sample preparation method.


Subject(s)
Cell-Derived Microparticles/metabolism , Protein Aggregates , Proteomics/methods , Animals , Cell Line, Tumor , Humans , Mice , Protein Processing, Post-Translational , RAW 264.7 Cells
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